2. Academic Validation
  3. A glyoxylate-containing benzene derivative and butenolides from a marine algicolous fungus Aspergillus sp. SCSIO 41304

A glyoxylate-containing benzene derivative and butenolides from a marine algicolous fungus Aspergillus sp. SCSIO 41304

  • Nat Prod Res. 2023 Feb;37(3):441-448. doi: 10.1080/14786419.2021.1978994.
Xin Qi 1 2,  Wei-Hao Chen 2 3,  Xiu-Ping Lin 2 3 4,  Sheng-Rong Liao 2 3 4,  Bin Yang 2 3 4,  Xue-Feng Zhou 2 3 4,  Yong-Hong Liu 2 3 4,  Jun-Feng Wang 2 3 4,  Yong Li 1
Affiliations

Affiliations

  • 1 School of Pharmaceutical Sciences, Changchun University of Chinese Medicine, Changchun, China.
  • 2 CAS Key Laboratory of Tropical Marine Bio-resources and Ecology/Guangdong Key Laboratory of Marine Materia Medica, Innovation Academy of South China Sea Ecology and Environmental Engineering, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou, China.
  • 3 Southern Marine Science and Engineering Guangdong Laboratory, South China Sea Institute of Oceanology Chinese Academy of Sciences, Guangzhou, China.
  • 4 Sanya Institute of Oceanology, SCSIO, Yazhou Scientific Bay, Sanya, China.
PMID: 34542359 DOI: 10.1080/14786419.2021.1978994
Abstract

A new glyoxylate-containing benzene derivative, methyl 2-(4-hydroxy-3-(3'-methyl-2'-butenyl)phenyl)-2-oxoacetate (1), together with ten known compounds (2-11), were isolated from the marine algicolous fungus, Aspergillus sp. SCSIO 41304. Their planar structures and absolute configurations were elucidated by detailed NMR, MS spectroscopic analysis and comparing with literature data. Compound 1 was isolated as a new Fungal secondary metabolite, possessing a methyl glyoxylate moiety R-CO-CO-OCH3, which is rare in natural sources. All the isolated compounds (1-11) were tested for their Antibacterial and enzyme inhibitory activities against acetylcholinesterase (AChE) and pancreatic Lipase (PL). Among these compounds, aspulvinone H (4) showed moderate inhibition against AChE and PL with IC50 values of 25.95 and 47.06 μM, respectively. Further molecular docking simulation exhibited that compound 4 could well bind to the catalytic pockets of the AChE and PL.

Keywords

Algicolous fungus; Aspergillus sp.; enzyme inhibitory activities; glyoxylate.

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